Merck
CN

SAE0090

Sigma-Aldrich

Beta-galactoside alpha-2,6-sialyltransferase 1

≥300 units/mg protein, ST6GAL1 human recombinant, expressed in HEK 293 cells

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别名:
Alpha 2,6-ST 1, B-cell antigen CD75, CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,6-sialyltransferase 1, ST6Gal I, Sialyltransferase 1

重组

expressed in HEK 293 cells

检测方案

≥95% (The specific activity of ST6Gal I is measured by its ability to transfer sialic acid from CMP-NANA to asialofetuin., SDS-PAGE)

形式

lyophilized powder

specific activity

≥300 units/mg protein

运输

ambient

储存温度

−20°C

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此商品
SAE0093S1951HPA018890
assay

≥95% (The specific activity of ST6Gal I is measured by its ability to transfer sialic acid from CMP-NANA to asialofetuin., SDS-PAGE)

assay

95% (SDS-PAGE)

assay

-

assay

-

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

form

buffered aqueous glycerol solution

specific activity

≥300 units/mg protein

specific activity

2000 units/mg protein

specific activity

≥2 units/mg protein

specific activity

-

shipped in

ambient

shipped in

ambient

shipped in

dry ice

shipped in

wet ice

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

一般描述

Recombinant human Beta-galactoside alpha-2,6-sialyltransferase 1 (ST6Gal I) is expressed in human HEK 293 cells as a glycoprotein with a calculated molecular mass of 43.5 kDa (amino acids 27-406). The DTT-reduced protein migrates as a ~50 kDa polypeptide on SDS-PAGE due to glycosylation. This protein is manufactured in human cells, with no serum. The human cells expression system allows human-like glycosylation and folding, and often supports higher specific activity of the protein. The protein is produced with no artificial tags.

生化/生理作用

ST6Gal I catalyzes the transfer of CMP-N-acetylneuraminate (CMP-sialic acid, CMP-NANA) to the β-D-galactosyl-1,4-N-acetyl-D-glucosaminyl termini on glycoproteins. Sialic acids are distributed in a variety of glycolipids and glycoproteins.1 The sialic acid that is added to a galactose (Gal) can be bound either to the hydroxyl attached to carbon-3 of Gal to form an α-2,3 glycosidic linkage, or to the hydroxyl group attached to carbon-6 to form an α-2,6 glycosidic linkage.1 ST6Gal I generates a α-2,6 linkage of sialic acid on the non-reducing, terminal Galβ1 4GlcNAc residues of oligosaccharides and glycoconjugates.2

Terminal sialylation has been shown to decrease Fcγ receptor binding and increase anti-inflammatory activity,3 as well as antibody-dependent cellular cytotoxicity in different studies by reduced binding of sialylated antibody towards FcγRIIIa.4-5

This recombinant ST6Gal I product can be used to study the mode of action of the enzyme, as well as its potential inhibitors. It can also be used as a glycoengineering tool to modify glycoproteins in vitro.

CMP-N-acetylneuraminate (CMP-sialic acid, CMP-NANA) to the β-D-galactosyl-1,4-N-acetyl-D-glucosaminyl termini on glycoproteins.
Sialic acids are distributed in a variety of glycolipids and glycoproteins. The sialic acid that is added to a galactose (Gal) can be bound either to the hydroxyl attached to carbon-3 of Gal to form an α-2,3 glycosidic linkage, or to the hydroxyl group attached to carbon-6 to form an α-2,6 glycosidic linkage. ST6Gal I generates a α-2,6 linkage of sialic acid on the non-reducing, terminal Galβ1 4GlcNAc residues of oligosaccharides and glycoconjugates.

Terminal sialylation has been shown to decrease Fcγ receptor binding and increase anti-inflammatory activity, as well as antibody-dependent cellular cytotoxicity in different studies by reduced binding of sialylated antibody towards FcγRIIIa.

单位定义

One unit is defined as the amount of enzyme required to transfer 1.0 nanomole of sialic acid from CMP-NANA to asialofetuin per minute at pH 6.0, 37oC.

储存分类代码

11 - Combustible Solids

WGK

WGK 2

闪点(°F)

Not applicable

闪点(°C)

Not applicable

法规信息

常规特殊物品

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Yoshikatsu Kaneko et al.
Science (New York, N.Y.), 313(5787), 670-673 (2006-08-05)
Immunoglobulin G (IgG) mediates pro- and anti-inflammatory activities through the engagement of its Fc fragment (Fc) with distinct Fcg receptors (FcgRs). One class of Fc-FcgR interactions generates pro-inflammatory effects of immune complexes and cytotoxic antibodies. In contrast, therapeutic intravenous gamma
J Weinstein et al.
The Journal of biological chemistry, 257(22), 13835-13844 (1982-11-25)
A Gal beta 1 to 4GlcNAc alpha 2 to 6 sialyltransferse and a Gal beta 1 to 3(4)GlcNAc alpha 2 to 3 sialyltransferase have been purified 23,000- and 860,000-fold to homogeneity from Triton CF-54 extracts of rat liver membranes. The
Bernard J Scallon et al.
Molecular immunology, 44(7), 1524-1534 (2006-10-19)
Although it is now clear that certain Fc glycan structures on immunoglobulin G (IgG) antibodies (Abs) can have a dramatic influence on binding to selected Fcgamma receptors (FcgammaR) and on Fc-mediated immune functions, the effects of all known Fc glycan
Michael F Naso et al.
mAbs, 2(5), 519-527 (2010-08-19)
Covalently-linked glycans on proteins have many functional roles, some of which are still not completely understood. Antibodies have a very specific glycan modification in the Fc region that is required for mediating immune effector functions. These Fc glycans are typically
Makoto Ogata et al.
BMC biotechnology, 9, 54-54 (2009-06-09)
Sialic acid is a deoxy uronic acid with a skeleton of nine carbons which is mostly found on cell surface in animals. This sialic acid on cell surface performs various biological functions by acting as a receptor for microorganisms, viruses

商品

Glycosyltransferases

Glycosyltransferases were initially considered to be specific for a single glycosyl donor and acceptor, which led to the one enzyme-one linkage concept. Subsequent observations have refuted the theory of absolute enzymatic specificity by describing the transfer of analogs of some nucleoside mono- or diphosphate sugar donors.

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